Recombinant Canine CD137 Protein (His Tag)

Name: Recombinant Canine CD137 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-0669
Availability: InStock

Collections: Cluster of differentiation (cd) proteins, Featured cd protein molecules, Recombinant proteins

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Product Overview

Tag	His
Host Species	Canine
Accession	XP_850336.1
Background	CD137 (also known as 4-1BB) is a surface co-stimulatory glycoprotein originally described as present on activated T lymphocytes, which belongs to the tumor necrosis factor (TNF) receptor superfamily. It is expressed mainly on activated CD4+ and CD8+ T cells, and binds to a high-affinity ligand (4-1BBL) expressed on several antigen-presenting cells such as macrophages and activated B cells. Upon ligand binding, 4-1BB is associated with the tumor necrosis factor receptor-associated factors (TRAFs), the adaptor protein which mediates downstream signaling events including the activation of NF-kappaB and cytokine production. 4-1BB signaling either by binding to 4-1BBL or by antibody ligation delivers signals for T-cell activation and growth, as well as monocyte proliferation and B-cell survival, and plays an important role in the amplification of T cell-mediated immune responses. In addition, CD137 and CD137L are expressed in different human primary tumor tissues, suggesting that they may influence the progression of tumors. Crosslinking of CD137 on activated T cells has shown promise in enhancing anti-tumor immune responses in murine models, and agonistic anti-CD137 antibodies are currently being tested in phase I clinical trials.Immune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsCo-stimulatory Immune Checkpoint Targets ImmunotherapyCancer ImmunotherapyTargeted Therapy
Description	A DNA sequence encoding the canine TNFRSF9 (XP_850336.1) (Met1-Ser185) was expressed with a C-terminal His tag.
Source	HEK293
Predicted N Terminal	Ile 24
AA Sequence	Met1-Ser185
Molecular Weight	The recombinant canine TNFRSF9 comprises 173 a.a. and has a predicted molecular mass of 18.4 kDa. The apparent molecular mass of the protein is approximately 28-34 kDa in SDS-PAGE under reducing conditions due to glycosylation.
Purity	>95% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Measured by its binding ability in a functional ELISA.Immobilized canine TNFRSF9-His at 10 ug/ml (100 ul/well) can bind rat Fc-TNFSF9, The EC50 of rat Fc-TNFSF9 is 0.26-0.62 ug/ml.
Formulation	Lyophilized from sterile PBS, pH 7.4..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.